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Showing 1–9 of 9 results
Advanced filters: Author: Björn M. Burmann Clear advanced filters

  • Chaperones interact with a canonical motif in α-synuclein, which can be prevented by phosphorylation of α-synuclein at Tyr39, whereas inhibition of this interaction leads to the localization of α-synuclein to the mitochondria and aggregate formation.

    • Björn M. Burmann
    • Juan A. Gerez
    • Sebastian Hiller
    Research
    Nature
    Volume: 577, P: 127-132

  • The bacterial chaperone Trigger Factor (TF) is a dynamic protein and its dimer structure is unknown. Here the authors present a protocol combining NMR, computational and biophysical methods for the structural characterization of large dynamic protein complexes and show that TF forms a symmetric head-to-tail dimer.

    • Leonor Morgado
    • Björn M. Burmann
    • Sebastian Hiller
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-11

  • The outer-membrane protein TamA is involved in autotransporter biogenesis in Escherichia coli. The crystal structure of TamA, determined to 2.3 Å, reveals a 16-strand β-barrel that is closed by a lid on its extracellular face. A weakened lateral wall in the barrel suggests the presence of a gate for substrate exit to the lipid bilayer.

    • Fabian Gruss
    • Franziska Zähringer
    • Timm Maier
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 1318-1320

  • Stress granules are non-membranous organelles connected to stress responses and age-related disease. Here, the authors identify a conserved yeast protein, Lsm7, that facilitates stress granule formation through dynamic liquid-liquid phase separation condensates upon 2-deoxy-D-glucose-induced stress.

    • Michelle Lindström
    • Lihua Chen
    • Beidong Liu
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-17

  • Using advanced solution NMR spectroscopy, Kawale and Burmann show that the carboxy-terminal region of the UvrD helicase adopts a Tudor-domain like fold to facilitate its interaction with RNA polymerase. This study provides molecular insights into the interaction between UvrD and RNA polymerase during DNA repair.

    • Ashish A. Kawale
    • Björn M. Burmann
    ResearchOpen Access
    Communications Biology
    Volume: 3, P: 1-13

  • Skp is a bacterial chaperone that prevents aggregation of outer membrane proteins as they traverse the periplasmic space. The conformation and dynamics of Skp in complex with two OMPs are now examined by NMR spectroscopy. The analyses reveal that Skp provides a scaffold for its substrates, which in turn populate a dynamic conformational ensemble.

    • Björn M Burmann
    • Congwei Wang
    • Sebastian Hiller
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 1265-1272